메뉴 건너뛰기




Volumn 81, Issue 15, 2007, Pages 8201-8210

Identification of two distinct human immunodeficiency virus type 1 vif determinants critical for interactions with human APOBEC3G and APOBEC3F

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3F; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; ARGININE; GLUTAMIC ACID; GLUTAMINE; METHIONINE; SERINE; VIF PROTEIN;

EID: 34547119261     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00395-07     Document Type: Article
Times cited : (200)

References (43)
  • 1
    • 1642367210 scopus 로고    scopus 로고
    • A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor
    • Bogerd, H. P., B. P. Doehle, H. L. Wiegand, and B. R. Cullen. 2004. A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor. Proc. Natl. Acad. Sci. USA 101:3770-3774.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3770-3774
    • Bogerd, H.P.1    Doehle, B.P.2    Wiegand, H.L.3    Cullen, B.R.4
  • 2
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello, S. G., R. S. Harris, and M. S. Neuberger. 2003. The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr. Biol. 13:2009-2013.
    • (2003) Curr. Biol , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 3
    • 0033856458 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120
    • Derdeyn, C. A., J. M. Decker, J. N. Sfakianos, X. Wu, W. A. O'Brien, L. Ratner, J. C. Kappes, G. M. Shaw, and E. Hunter. 2000. Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120. J. Virol. 74:8358-8367.
    • (2000) J. Virol , vol.74 , pp. 8358-8367
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Wu, X.4    O'Brien, W.A.5    Ratner, L.6    Kappes, J.C.7    Shaw, G.M.8    Hunter, E.9
  • 4
    • 14844337426 scopus 로고    scopus 로고
    • The tyrosine kinases Fyn and Hck favor the recruitment of tyrosine-phosphorylated APOBEC3G into vif-defective HIV-1 particles
    • Douaisi, M., S. Dussart, M. Courcoul, G. Bessou, E. C. Lerner, E. Decroly, and R. Vigne. 2005. The tyrosine kinases Fyn and Hck favor the recruitment of tyrosine-phosphorylated APOBEC3G into vif-defective HIV-1 particles. Biochem. Biophys. Res. Commun. 329:917-924.
    • (2005) Biochem. Biophys. Res. Commun , vol.329 , pp. 917-924
    • Douaisi, M.1    Dussart, S.2    Courcoul, M.3    Bessou, G.4    Lerner, E.C.5    Decroly, E.6    Vigne, R.7
  • 5
    • 0037225677 scopus 로고    scopus 로고
    • Amino acid residues 88 and 89 in the central hydrophilic region of human immunodeficiency virus type 1 Vif are critical for viral infectivity by enhancing the steady-state expression of Vif
    • Fujita, M., A. Sakurai, A. Yoshida, M. Miyaura, A. H. Koyama, K. Sakai, and A. Adachi. 2003. Amino acid residues 88 and 89 in the central hydrophilic region of human immunodeficiency virus type 1 Vif are critical for viral infectivity by enhancing the steady-state expression of Vif. J. Virol. 77:1626-1632.
    • (2003) J. Virol , vol.77 , pp. 1626-1632
    • Fujita, M.1    Sakurai, A.2    Yoshida, A.3    Miyaura, M.4    Koyama, A.H.5    Sakai, K.6    Adachi, A.7
  • 6
    • 0026649561 scopus 로고    scopus 로고
    • + T lymphocytes. J. Virol. 66:6489-6495.
    • + T lymphocytes. J. Virol. 66:6489-6495.
  • 7
    • 0027953516 scopus 로고
    • Subcellular localization of the Vif protein of human immunodeficiency virus type 1
    • Goncalves, J., P. Jallepalli, and D. H. Gabuzda. 1994. Subcellular localization of the Vif protein of human immunodeficiency virus type 1. J. Virol. 68:704-712.
    • (1994) J. Virol , vol.68 , pp. 704-712
    • Goncalves, J.1    Jallepalli, P.2    Gabuzda, D.H.3
  • 9
    • 0142092452 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity
    • Kao, S., M. A. Khan, E. Miyagi, R. Plishka, A. Buckler-White, and K. Strebel. 2003. The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity. J. Virol. 77:11398-11407.
    • (2003) J. Virol , vol.77 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3    Plishka, R.4    Buckler-White, A.5    Strebel, K.6
  • 10
    • 21444439295 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function
    • Kobayashi, M., A. Takaori-Kondo, Y. Miyauchi, K. Iwai, and T. Uchiyama. 2005. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. J. Biol. Chem. 280:18573-18578.
    • (2005) J. Biol. Chem , vol.280 , pp. 18573-18578
    • Kobayashi, M.1    Takaori-Kondo, A.2    Miyauchi, Y.3    Iwai, K.4    Uchiyama, T.5
  • 11
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier, D., F. Bouchonnet, F. Clavel, and A. J. Hance. 2003. Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 300:1112.
    • (2003) Science , vol.300 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 12
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament, M. T., W. L. Brown, A. J. Schumacher, and R. S. Harris. 2004. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr. Biol. 14:1385-1391.
    • (2004) Curr. Biol , vol.14 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 13
    • 0842347676 scopus 로고    scopus 로고
    • Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G
    • Liu, B., X. Yu, K. Luo, Y. Yu, and X. F. Yu. 2004. Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G. J. Virol. 78:2072-2081.
    • (2004) J. Virol , vol.78 , pp. 2072-2081
    • Liu, B.1    Yu, X.2    Luo, K.3    Yu, Y.4    Yu, X.F.5
  • 14
    • 23844473725 scopus 로고    scopus 로고
    • Primate lentiviral virion infectivity factors arc substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G
    • Luo, K., Z. Xiao, E. Ehrlich, Y. Yu, B. Liu, S. Zheng, and X. F. Yu. 2005. Primate lentiviral virion infectivity factors arc substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc. Natl. Acad. Sci. USA 102:11444-11449.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11444-11449
    • Luo, K.1    Xiao, Z.2    Ehrlich, E.3    Yu, Y.4    Liu, B.5    Zheng, S.6    Yu, X.F.7
  • 15
    • 0031797865 scopus 로고    scopus 로고
    • An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein
    • Madani, N., and D. Kabat. 1998. An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. J. Virol. 72:10251-10255.
    • (1998) J. Virol , vol.72 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 16
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat, B., P. Turelli, G. Caron, M. Friedli, L. Perrin, and D. Trono. 2003. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424:99-103.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 17
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat, B., P. Turelli, S. Liao, and D. Trono. 2004. A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J. Biol. Chem. 279:14481-14483.
    • (2004) J. Biol. Chem , vol.279 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 18
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin, M., K. M. Rose, S. L. Kozak, and D. Kabat. 2003. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 9:1398-1403.
    • (2003) Nat. Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 19
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle, A., B. Strack, P. Ancuta, C. Zhang, M. McPike, and D. Gabuzda. 2004. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279:7792-7798.
    • (2004) J. Biol. Chem , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 20
    • 1342343136 scopus 로고    scopus 로고
    • Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression
    • Nguyen, K. L., M. Ilano, H. Akari, E. Miyagi, E. M. Poeschla, K. Strebel, and S. Bour. 2004. Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression. Virology 319:163-175.
    • (2004) Virology , vol.319 , pp. 163-175
    • Nguyen, K.L.1    Ilano, M.2    Akari, H.3    Miyagi, E.4    Poeschla, E.M.5    Strebel, K.6    Bour, S.7
  • 21
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • Schrofelbauer, B., D. Chen, and N. R. Landau. 2004. A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proc. Natl. Acad. Sci. USA 101:3927-3932.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 22
    • 33744939997 scopus 로고    scopus 로고
    • Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G
    • Schrofelbauer, B., T. Senger, G. Manning, and N. R. Landau. 2006. Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G. J. Virol. 80: 5984-5991.
    • (2006) J. Virol , vol.80 , pp. 5984-5991
    • Schrofelbauer, B.1    Senger, T.2    Manning, G.3    Landau, N.R.4
  • 23
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy, A. M., N. C. Gaddis, J. D. Choi, and M. H. Malim. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 24
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy, A. M., N. C. Gaddis, and M. H. Malim. 2003. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9:1404-1407.
    • (2003) Nat. Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 25
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • Simon, J. H., N. C. Gaddis, R. A. Fouchier, and M. H. Malim. 1998. Evidence for a newly discovered cellular anti-HIV-1 phenotype. Nat. Med. 4:1397-1400.
    • (1998) Nat. Med , vol.4 , pp. 1397-1400
    • Simon, J.H.1    Gaddis, N.C.2    Fouchier, R.A.3    Malim, M.H.4
  • 26
    • 0033053198 scopus 로고    scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Vif protein
    • Simon, J. H., A. M. Sheehy, E. A. Carpenter, R. A. Fouchier, and M. H. Malim. 1999. Mutational analysis of the human immunodeficiency virus type 1 Vif protein. J. Virol. 73:2675-2681.
    • (1999) J. Virol , vol.73 , pp. 2675-2681
    • Simon, J.H.1    Sheehy, A.M.2    Carpenter, E.A.3    Fouchier, R.A.4    Malim, M.H.5
  • 27
    • 67649888155 scopus 로고    scopus 로고
    • Natural variation in Vif: Differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification
    • Simon, V., V. Zennou, D. Murray, Y. Huang, D. D. Ho, and P. D. Bieniasz. 2005. Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification. PLoS Pathogens 1:e6.
    • (2005) PLoS Pathogens , vol.1
    • Simon, V.1    Zennou, V.2    Murray, D.3    Huang, Y.4    Ho, D.D.5    Bieniasz, P.D.6
  • 28
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak, K., C. de Noronha, W. Yonemoto, and W. C. Greene. 2003. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 12:591-601.
    • (2003) Mol. Cell , vol.12 , pp. 591-601
    • Stopak, K.1    de Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 29
  • 30
    • 4143124683 scopus 로고    scopus 로고
    • Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-likc 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs
    • Svarovskaia, E. S., H. Xu, J. L. Mbisa, R. Barr, R. J. Gorelick, A. Ono, E. O. Freed, W. S. Hu, and V. K. Pathak. 2004. Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-likc 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs. J. Biol. Chem. 279:35822-35828.
    • (2004) J. Biol. Chem , vol.279 , pp. 35822-35828
    • Svarovskaia, E.S.1    Xu, H.2    Mbisa, J.L.3    Barr, R.4    Gorelick, R.J.5    Ono, A.6    Freed, E.O.7    Hu, W.S.8    Pathak, V.K.9
  • 31
    • 33644752777 scopus 로고    scopus 로고
    • Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F
    • Tian, C., X. Yu, W. Zhang, T. Wang, R. Xu, and X. F. Yu. 2006. Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. J. Virol. 80:3112-3115.
    • (2006) J. Virol , vol.80 , pp. 3112-3115
    • Tian, C.1    Yu, X.2    Zhang, W.3    Wang, T.4    Xu, R.5    Yu, X.F.6
  • 32
    • 0033532628 scopus 로고    scopus 로고
    • Cytokine signals are sufficient for HIV-1 infection of resting human T lymphocytes
    • Unutmaz, D., V. N. KewalRamani, S. Marmon, and D. R. Littman. 1999. Cytokine signals are sufficient for HIV-1 infection of resting human T lymphocytes. J. Exp. Med. 189:1735-1746.
    • (1999) J. Exp. Med , vol.189 , pp. 1735-1746
    • Unutmaz, D.1    KewalRamani, V.N.2    Marmon, S.3    Littman, D.R.4
  • 33
    • 0027179103 scopus 로고
    • Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells
    • von Schwedler, U., J. Song, C. Aiken, and D. Trono. 1993. Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells. J. Virol. 67:4945-4955.
    • (1993) J. Virol , vol.67 , pp. 4945-4955
    • von Schwedler, U.1    Song, J.2    Aiken, C.3    Trono, D.4
  • 35
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand, H. L., B. P. Doehle, H. P. Bogerd, and B. R. Cullen. 2004. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23:2451-2458.
    • (2004) EMBO J , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 36
    • 33845996549 scopus 로고    scopus 로고
    • Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G
    • Xiao, Z., E. Ehrlich, K. Luo, Y. Xiong, and X. F. Yu. 2007. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. FASEB J. 21:217-222.
    • (2007) FASEB J , vol.21 , pp. 217-222
    • Xiao, Z.1    Ehrlich, E.2    Luo, K.3    Xiong, Y.4    Yu, X.F.5
  • 38
    • 1842732157 scopus 로고    scopus 로고
    • A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion
    • Xu, H., E. S. Svarovskaia, R. Barr, Y. Zhang, M. A. Khan, K. Strebel, and V. K. Pathak. 2004. A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Proc. Natl. Acad. Sci. USA 101:5652-5657.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5652-5657
    • Xu, H.1    Svarovskaia, E.S.2    Barr, R.3    Zhang, Y.4    Khan, M.A.5    Strebel, K.6    Pathak, V.K.7
  • 40
    • 0028705684 scopus 로고
    • Generation of high-titer pseudotyped retroviral vectors with very broad host range
    • Yee, J. K., T. Friedmann, and J. C. Burns. 1994. Generation of high-titer pseudotyped retroviral vectors with very broad host range. Methods Cell Biol. 43(Pt. A):99-112.
    • (1994) Methods Cell Biol , vol.43 , Issue.PART. A , pp. 99-112
    • Yee, J.K.1    Friedmann, T.2    Burns, J.C.3
  • 41
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X. F. Yu. 2003. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302:1056-1060.
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7
  • 42
    • 33646508336 scopus 로고    scopus 로고
    • Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates
    • Zennou, V., and P. D. Bieniasz. 2006. Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates. Virology 349:31-40.
    • (2006) Virology , vol.349 , pp. 31-40
    • Zennou, V.1    Bieniasz, P.D.2
  • 43
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang, H., B. Yang, R. J. Pomerantz, C. Zhang, S. C. Amnachalam, and L. Gao. 2003. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424:94-98.
    • (2003) Nature , vol.424 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Amnachalam, S.C.5    Gao, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.